ID A0A0M3QX48_DROBS Unreviewed; 1370 AA.
AC A0A0M3QX48;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=chitin synthase {ECO:0000256|ARBA:ARBA00012543};
DE EC=2.4.1.16 {ECO:0000256|ARBA:ARBA00012543};
DE Flags: Fragment;
GN ORFNames=Dbus_chr3Lg2405 {ECO:0000313|EMBL:ALC45239.1};
OS Drosophila busckii (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=30019 {ECO:0000313|EMBL:ALC45239.1, ECO:0000313|Proteomes:UP000494163};
RN [1] {ECO:0000313|EMBL:ALC45239.1, ECO:0000313|Proteomes:UP000494163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole larvae {ECO:0000313|EMBL:ALC45239.1};
RA Zhou Q., Bachtrog D.;
RT "Ancestral chromatin configuration constrains chromatin evolution on
RT differentiating sex chromosomes in Drosophila.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-
CC D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+1) + H(+) +
CC UDP; Xref=Rhea:RHEA:16637, Rhea:RHEA-COMP:9593, Rhea:RHEA-COMP:9595,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17029, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=2.4.1.16;
CC Evidence={ECO:0000256|ARBA:ARBA00000319};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP012525; ALC45239.1; -; Genomic_DNA.
DR STRING; 30019.A0A0M3QX48; -.
DR OMA; CKIKIQV; -.
DR Proteomes; UP000494163; Chromosome 3l sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004100; F:chitin synthase activity; IEA:UniProtKB-EC.
DR CDD; cd04190; Chitin_synth_C; 1.
DR InterPro; IPR004835; Chitin_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22914; CHITIN SYNTHASE; 1.
DR PANTHER; PTHR22914:SF14; CHITIN SYNTHASE; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000494163};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 223..249
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 886..911
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 917..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 941..966
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 972..990
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 997..1022
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1105..1124
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1164..1185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1321..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ALC45239.1"
SQ SEQUENCE 1370 AA; 156756 MW; B93DDF507D3CB911 CRC64;
KARDKPPLWD SFQDPPAKRT SGSDAHWKKL QFVLKLLKLF TYLLVFAVIL ACSVTAKLVY
LYMAGNTNGE VKVRVCSKYL DGQVTATRSK LEQIAWVWAL IFAFAAPELF TFLRALRITL
FKREQRPSGL EVALVTLFEL LHVVGLALIT FTVLPQLDVT RGAMLGCCVC FVPALLNILT
GTRFQWKSAD TLVNVASILA VVAQGSVFLV WPAMSSQLEL QLLALPLLLV SFRWWENYAN
TLASIAYIIR TIRCTRSRYH TYLYVAPLKM AVFGLLGFLL HGENFKEYFT LFFEAWQPHT
ITLTYTDGLR DTRPLPSNGS SFIKPTTFVS QYPLQSNAWA VVYALLVQVS AAYLCHIFGK
FACKIKIQHF SFALPLSLAT PVTVVAATLL SQLRAQDICA LHSLLPDYLT LQPLGESVAQ
LGALSLQYAL WLWPLWWLAQ LWTSWHIWHT HNDKNAPTEK LFVCPWYSGL LVDQCTMMNR
RILDWSDEYL AIKSDLTAAR DPAVALAADI NANASRDIQE TDKIPQLIVC ATMWHETEDE
MMEFLKSIVR LDEDQCARRL AKTHLNGGKA DDEYYELETN IFFEDAFVLD PRHCQNKRNP
PLNEYVKTLT RTIDKAVFEI YGVNIKIKPP LKIETPYGGR LVWTLPGRTK MVAHLKNKDK
IRHKKRWSQV MYMYYLLGFR IMETEQLSAR RKAVIAENTF LLALEGDIDF QPHAVQLLID
RMKAIDELGA ACGRIHPVGR GPMVWYQKFE YAIGHWLQKA TEHVIGCVLC SPGCFSLFRA
SALMENSVMK RYTLVTSEAM KMVQYDQGED RWLCTLLLKQ GSRVEYCAAS DAYTHSPEYF
NEFYNQRRRW VPSTMANIYD ILADADTVVK KNNSISTLYI MYQGMLMLGT VLGPGTIFLM
MVGALVAVFS IDIWTAFLWN FFPILCFILS CVYLKQKFQL LIAFVISAIY CLVMMAVLIG
IVVQMIEDGP LAPASMFFLL VAVQITLAGL MHPQEFLALL CGIIYYITIP SMYMLLMIYS
VFNMNDVSWG TREGPVLRDD DGESVEPHLP GWLNDPLLID SELGEVSLVE QRFWKDLIKQ
YLKPLELSKE QKQSMDDDLK ELRNMIAFAF VMVNAIFVLI VFLLQLKKDY LHLKWPIDPT
DFITFDRDNL QVDIYRQYKE LDPIGLCFVV FFGVILVIQF IAMFFHRFGT MSQLLATVQL
NWFRSNSQLS DEDAALELSG NAVNIARRLQ RPRRLFDEDE LDSNHYDELS VGQEDNHRES
MVRRQTICRL HESRNAEHSD YSDLVRNFER RFFGEADLNV RNLPLSRKSV KLLQQRRSVA
KENAAAMPGG TPTPKPGLRP PLLPVNAKKV SFRANTMEIY DNGGYEHTEF
//
